ID A0A3S2UWD9_9BURK Unreviewed; 713 AA.
AC A0A3S2UWD9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN ORFNames=EOD73_10385 {ECO:0000313|EMBL:RVT86507.1};
OS Inhella crocodyli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Inhella.
OX NCBI_TaxID=2499851 {ECO:0000313|EMBL:RVT86507.1, ECO:0000313|Proteomes:UP000288587};
RN [1] {ECO:0000313|EMBL:RVT86507.1, ECO:0000313|Proteomes:UP000288587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP-18 {ECO:0000313|EMBL:RVT86507.1,
RC ECO:0000313|Proteomes:UP000288587};
RA Chen W.-M.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC EC=6.1.1.14; Evidence={ECO:0000256|ARBA:ARBA00000201,
CC ECO:0000256|HAMAP-Rule:MF_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RVT86507.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SACM01000002; RVT86507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2UWD9; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000288587; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR NCBIfam; TIGR00211; glyS; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00255};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00255};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Reference proteome {ECO:0000313|Proteomes:UP000288587}.
FT DOMAIN 605..702
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 713 AA; 76162 MW; A7E187A464B197FD CRC64;
MMSTANLLVE LFVEELPPKA LKKLGDSFAQ LIADALRAQG LAGEGAVTPF ASPRRLGVHI
AGVAAKAADK AVRIKLMPVA VGLTPEGQPS PALLKKLAAS GLPADAPLER ALDGKAEALF
ANTVQPGASL AQGLQQALND MLKALPIPKV MSYQLADGWT NVHFVRPAHG LVALHGADRV
PVSLLGLEAG TTTRGHRFEA LDPLVTVPHA DAYADTLRSR GAVIASFAER REAIRGQLQA
AGAKLGLTPI DDEALLDEVT ALVERPNVLT CAFEEEFLAV PQECLILTMK ANQKYFPLLD
AQGKLTRHFL VVSNIAPDDA SAVVQGNERV VRPRLADAKF FYDQDRKKTL AERVPGLAKV
VYHGSLGSQG ERAERVRAIA HAIVNQLRTA TVPFTVDAKD QFDVLDSKVQ QAAQLAKADL
LTDMVGEFPE LQGIMGAYYA RHEGLRDGVA IAIEDHYKPR FAGDALPRNH TGTVLALADK
LETLVGLFGI GQLPTGDKDP FALRRHALGV IRILMEKNLP LSLPELVRAG LQAFPEGMLT
HASAADDLLH FAYERLTGAL REQGYSAQEV DAVIALRPSP WGDIPKRLAA VRAFAALPES
ASLAAANKRV GNILKKSDEA PVALNDALLQ EPAEAQLAAA LRAAAAQAQP LFEQGDYAAS
LQALAVLKAP VDAFFDAVMV NADDAALRAN RLALLRGLHE AMNRVADLSR LAH
//
